The three-dimensional structure of canine parvovirus and its functional implications

• Published in: Science (American Association for the Advancement of Science) Vol. 251; no. 5000; pp. 1456 - 1464
• Main Authors: Tsao, J. (Purdue University, West Lafayette, IN), Chapman, M.S, Agbandje, M, Keller, W, Smith, K, Wu, H, Luo, M, Smith, T.J, Rossmann, M.G, Compans, R.W
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for the Advancement of Science 22.03.1991; American Association for the Advancement of Science; The American Association for the Advancement of Science
• Subjects: ADN; Amino Acid Sequence; Amino acids; Analysis; Antigens, Viral - chemistry; Atomic structure; Base sequence; Biochemistry; Biological and medical sciences; Canine parvovirus; Canyons; Capsid; Capsid - ultrastructure; Capsid proteins; Crystallography; Crystals; Deoxyribonucleic acid; DNA; DNA, Viral - ultrastructure; Dogs; Electrical phases; Electron density; Electronic structure; Fundamental and applied biological sciences. Psychology; Genetics; GENOMAS; GENOME; Hemagglutinins, Viral - chemistry; Microbiology; Models, Molecular; Molecular Sequence Data; Molecular Structure; Morphology, structure, chemical composition, physicochemical properties; Nucleotide sequence; PARVOVIRIDAE; Parvoviridae - ultrastructure; PEPTIDE; PEPTIDOS; PROTEINAS; PROTEINE; Research Article; Viral morphology; Virion - ultrastructure; Virology; Virus Replication; Viruses; X-Ray Diffraction; Virus; Canine parvovirus; Parvovirus; Molecular structure; Virion; Parvoviridae; Property structure relationship; Subunit; Spatial structure
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.2006420

The three-dimensional atomic structure of a single-stranded DNA virus has been determined. Infectious virions of canine parvovirus contain 60 protein subunits that are predominantly VP-2. The central structural motif of VP-2 has the same topology (an eight-stranded antiparallel beta barrel) as has been found in many other icosahedral viruses but represents only about one-third of the capsid protein. There is a 22 angstrom long protrusion on the threefold axes, a 15 angstrom deep canyon circulating about each of the five cylindrical structures at the fivefold axes, and a 15 angstrom deep depression at the twofold axes. By analogy with rhinoviruses, the canyon may be the site of receptor attachment. Residues related to the antigenic properties of the virus are found on the threefold protrusions. Some of the amino termini of VP-2 run to the exterior in full but not empty virions, which is consistent with the observation that some VP-2 polypeptides in full particles can be cleaved by trypsin. Eleven nucleotides are seen in each of 60 symmetry-related pockets on the interior surface of the capsid and together account for 13 percent of the genome